PMID:1092361
| Citation |
Bitar, KG (1975) The primary structure of the ribosomal protein L29 from Escherichia coli. Biochim. Biophys. Acta 386:99-106 |
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| Abstract |
The amino acid sequence of ribosomal protein L29 was determined utilizing an improved Beckman sequenator, a solid phase peptide sequenator, and more conventional techniques. L29 is composed of 63 amino acid residues and has a molecular weight of 7262. It lacks proline, cysteine, isoleucine, tyrosine and tryptophan. The N-terminal and C-terminal regions (residues 1-9 and 50-63) are basic, while the rest of the molecule is hydrophobic and neutral. Calculated P-a values show two helical regions: one from residues 1 through 32 and the other from residues 37 through 47. No beta-sheet regions are predicted. Short identical regions occur within the sequence of L29 as well as between L29 and other ribosomal proteins. |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acids/analysis; Bacterial Proteins; Escherichia coli/analysis; Peptide Fragments/analysis; Peptide Hydrolases; Protein Conformation; Ribosomes/analysis; Staphylococcus/enzymology; Thermolysin; Trypsin |
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